P32019 (I5P2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Type II inositol-1,4,5-trisphosphate 5-phosphatase
EC=3.1.3.36

Alternative name(s):
75 kDa inositol polyphosphate-5-phosphatase
Phosphoinositide 5-phosphatase
Short name=5PTase

Gene names

Name:

INPP5B

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	993 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events.
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.
Subunit structure	Interacts with FAM109A and FAM109B. Ref.6 Ref.7
Subcellular location	Cytoplasm › cytosol. Membrane; Peripheral membrane protein; Cytoplasmic side.
Tissue specificity	Platelets.
Post-translational modification	Isoprenylation at Cys-990 may be required for localization at the membrane.
Sequence similarities	Belongs to the inositol-1,4,5-trisphosphate 5-phosphatase type II family. Contains 1 Rho-GAP domain.
Sequence caution	The sequence AAA79207.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase
PTM	Lipoprotein Prenylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	regulation of small GTPase mediated signal transduction Traceable author statement. Source: Reactome small GTPase mediated signal transduction Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome integral to membrane Non-traceable author statement. Source: UniProtKB microtubule cytoskeleton Inferred from direct assay. Source: HPA
Molecular function	inositol-polyphosphate 5-phosphatase activity Non-traceable author statement. Source: UniProtKB phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction Ref.7. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P32019-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation available.

Isoform 2 (identifier: P32019-2)

The sequence of this isoform differs from the canonical sequence as follows:
     178-257: Missing.

Isoform 3 (identifier: P32019-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-244: Missing.

Isoform 4 (identifier: P32019-4)

The sequence of this isoform differs from the canonical sequence as follows:
     810-828: TLMPVWTGDDGSQLDSPME → LAYLAAYCFETQLVTKSLI
     829-993: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 320

320

PRO_0000015639

Chain

321 – 993

673

Type II inositol-1,4,5-trisphosphate 5-phosphatase

PRO_0000015640

Regions

Domain

821 – 993

173

Rho-GAP

Region

459 – 460

2

Substrate

Region

582 – 583

2

Substrate binding

Region

596 – 598

3

Substrate binding

Sites

Binding site

383

1

Substrate

Amino acid modifications

Lipidation

990

1

S-farnesyl cysteine Potential

Natural variations

Alternative sequence

1 – 244

244

Missing in isoform 3.

VSP_012821

Alternative sequence

178 – 257

80

Missing in isoform 2.

VSP_012820

Alternative sequence

810 – 828

19

TLMPV…DSPME → LAYLAAYCFETQLVTKSLI in isoform 4.

VSP_013902

Alternative sequence

829 – 993

165

Missing in isoform 4.

VSP_013903

Natural variant

46

1

G → S.
Corresponds to variant rs56993041 [ dbSNP | Ensembl ].

VAR_061270

Natural variant

745

1

M → T. Ref.1 Ref.3 Ref.5
Corresponds to variant rs11488569 [ dbSNP | Ensembl ].

VAR_028002

Experimental info

Mutagenesis

990

1

C → S: Loss of prenylation and membrane localization.

Sequence conflict

587 – 606

20

GSDDW…WCDRI → RALTTGIPVRSAVLLPGVIG F AA sequence Ref.5

Sequence conflict

911

1

G → P AA sequence Ref.5

Secondary structure

1

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993

Helix Strand Turn

Details...

Beta strand

340 – 349

10

Helix

364 – 367

4

Beta strand

375 – 379

5

Helix

388 – 391

4

Helix

398 – 407

10

Beta strand

416 – 423

8

Beta strand

428 – 434

7

Helix

435 – 440

6

Beta strand

441 – 447

7

Beta strand

464 – 469

6

Beta strand

472 – 478

7

Helix

485 – 487

3

Helix

488 – 501

14

Beta strand

509 – 511

3

Beta strand

518 – 525

8

Helix

537 – 545

9

Helix

549 – 553

5

Helix

557 – 563

7

Beta strand

607 – 609

3

Beta strand

614 – 620

7

Beta strand

626 – 629

4

Beta strand

632 – 638

7

Beta strand

640 – 643

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 15, 2009. Version 4. Checksum: ABD3581CC6CD29D6	FASTA	993	112,852
	10 20 30 40 50 60 MDQSVAIQET LAEGEYCVIA VQGVLCEGDS RQSRLLGLVR YRLEHGGQEH ALFLYTHRRM 70 80 90 100 110 120 AITGDDVSLD QIVPVSRDFT LEEVSPDGEL YILGSDVTVQ LDTAELSLVF QLPFGSQTRM 130 140 150 160 170 180 FLHEVARACP GFDSATRDPE FLWLSRYRCA ELELEMPTPR GCNSALVTWP GYATIGGGRY 190 200 210 220 230 240 PSRKKRWGLE EARPQGAGSV LFWGGAMEKT GFRLMERAHG GGFVWGRSAR DGRRDEELEE 250 260 270 280 290 300 AGREMSAAAG SRERNTAGGS NFDGLRPNGK GVPMDQSSRG QDKPESLQPR QNKSKSEITD 310 320 330 340 350 360 MVRSSTITVS DKAHILSMQK FGLRDTIVKS HLLQKEEDYT YIQNFRFFAG TYNVNGQSPK 370 380 390 400 410 420 ECLRLWLSNG IQAPDVYCVG FQELDLSKEA FFFHDTPKEE EWFKAVSEGL HPDAKYAKVK 430 440 450 460 470 480 LIRLVGIMLL LYVKQEHAAY ISEVEAETVG TGIMGRMGNK GGVAIRFQFH NTSICVVNSH 490 500 510 520 530 540 LAAHIEEYER RNQDYKDICS RMQFCQPDPS LPPLTISNHD VILWLGDLNY RIEELDVEKV 550 560 570 580 590 600 KKLIEEKDFQ MLYAYDQLKI QVAAKTVFEG FTEGELTFQP TYKYDTGSDD WDTSEKCRAP 610 620 630 640 650 660 AWCDRILWKG KNITQLSYQS HMALKTSDHK PVSSVFDIGV RVVNDELYRK TLEEIVRSLD 670 680 690 700 710 720 KMENANIPSV SLSKREFCFQ NVKYMQLKVE SFTIHNGQVP CHFEFINKPD EESYCKQWLN 730 740 750 760 770 780 ANPSRGFLLP DSDVEIDLEL FVNKMTATKL NSGEDKIEDI LVLHLDRGKD YFLSVSGNYL 790 800 810 820 830 840 PSCFGSPIHT LCYMREPILD LPLETISELT LMPVWTGDDG SQLDSPMEIP KELWMMVDYL 850 860 870 880 890 900 YRNAVQQEDL FQQPGLRSEF EHIRDCLDTG MIDNLSASNH SVAEALLLFL ESLPEPVICY 910 920 930 940 950 960 STYHNCLECS GNYTASKQVI STLPIFHKNV FHYLMAFLRE LLKNSAKNHL DENILASIFG 970 980 990 SLLLRNPAGH QKLDMTEKKK AQEFIHQFLC NPL
	Isoform 2 [UniParc]. Checksum: 4882C26F6E4DC9C6	FASTA	913	103,987
	10 20 30 40 50 60 MDQSVAIQET LAEGEYCVIA VQGVLCEGDS RQSRLLGLVR YRLEHGGQEH ALFLYTHRRM 70 80 90 100 110 120 AITGDDVSLD QIVPVSRDFT LEEVSPDGEL YILGSDVTVQ LDTAELSLVF QLPFGSQTRM 130 140 150 160 170 180 FLHEVARACP GFDSATRDPE FLWLSRYRCA ELELEMPTPR GCNSALVTWP GYATIGGGGS 190 200 210 220 230 240 NFDGLRPNGK GVPMDQSSRG QDKPESLQPR QNKSKSEITD MVRSSTITVS DKAHILSMQK 250 260 270 280 290 300 FGLRDTIVKS HLLQKEEDYT YIQNFRFFAG TYNVNGQSPK ECLRLWLSNG IQAPDVYCVG 310 320 330 340 350 360 FQELDLSKEA FFFHDTPKEE EWFKAVSEGL HPDAKYAKVK LIRLVGIMLL LYVKQEHAAY 370 380 390 400 410 420 ISEVEAETVG TGIMGRMGNK GGVAIRFQFH NTSICVVNSH LAAHIEEYER RNQDYKDICS 430 440 450 460 470 480 RMQFCQPDPS LPPLTISNHD VILWLGDLNY RIEELDVEKV KKLIEEKDFQ MLYAYDQLKI 490 500 510 520 530 540 QVAAKTVFEG FTEGELTFQP TYKYDTGSDD WDTSEKCRAP AWCDRILWKG KNITQLSYQS 550 560 570 580 590 600 HMALKTSDHK PVSSVFDIGV RVVNDELYRK TLEEIVRSLD KMENANIPSV SLSKREFCFQ 610 620 630 640 650 660 NVKYMQLKVE SFTIHNGQVP CHFEFINKPD EESYCKQWLN ANPSRGFLLP DSDVEIDLEL 670 680 690 700 710 720 FVNKMTATKL NSGEDKIEDI LVLHLDRGKD YFLSVSGNYL PSCFGSPIHT LCYMREPILD 730 740 750 760 770 780 LPLETISELT LMPVWTGDDG SQLDSPMEIP KELWMMVDYL YRNAVQQEDL FQQPGLRSEF 790 800 810 820 830 840 EHIRDCLDTG MIDNLSASNH SVAEALLLFL ESLPEPVICY STYHNCLECS GNYTASKQVI 850 860 870 880 890 900 STLPIFHKNV FHYLMAFLRE LLKNSAKNHL DENILASIFG SLLLRNPAGH QKLDMTEKKK 910 AQEFIHQFLC NPL
	Isoform 3 [UniParc]. Checksum: 50921FAACF7E1E39	FASTA	749	85,620
	10 20 30 40 50 60 MSAAAGSRER NTAGGSNFDG LRPNGKGVPM DQSSRGQDKP ESLQPRQNKS KSEITDMVRS 70 80 90 100 110 120 STITVSDKAH ILSMQKFGLR DTIVKSHLLQ KEEDYTYIQN FRFFAGTYNV NGQSPKECLR 130 140 150 160 170 180 LWLSNGIQAP DVYCVGFQEL DLSKEAFFFH DTPKEEEWFK AVSEGLHPDA KYAKVKLIRL 190 200 210 220 230 240 VGIMLLLYVK QEHAAYISEV EAETVGTGIM GRMGNKGGVA IRFQFHNTSI CVVNSHLAAH 250 260 270 280 290 300 IEEYERRNQD YKDICSRMQF CQPDPSLPPL TISNHDVILW LGDLNYRIEE LDVEKVKKLI 310 320 330 340 350 360 EEKDFQMLYA YDQLKIQVAA KTVFEGFTEG ELTFQPTYKY DTGSDDWDTS EKCRAPAWCD 370 380 390 400 410 420 RILWKGKNIT QLSYQSHMAL KTSDHKPVSS VFDIGVRVVN DELYRKTLEE IVRSLDKMEN 430 440 450 460 470 480 ANIPSVSLSK REFCFQNVKY MQLKVESFTI HNGQVPCHFE FINKPDEESY CKQWLNANPS 490 500 510 520 530 540 RGFLLPDSDV EIDLELFVNK MTATKLNSGE DKIEDILVLH LDRGKDYFLS VSGNYLPSCF 550 560 570 580 590 600 GSPIHTLCYM REPILDLPLE TISELTLMPV WTGDDGSQLD SPMEIPKELW MMVDYLYRNA 610 620 630 640 650 660 VQQEDLFQQP GLRSEFEHIR DCLDTGMIDN LSASNHSVAE ALLLFLESLP EPVICYSTYH 670 680 690 700 710 720 NCLECSGNYT ASKQVISTLP IFHKNVFHYL MAFLRELLKN SAKNHLDENI LASIFGSLLL 730 740 RNPAGHQKLD MTEKKKAQEF IHQFLCNPL
	Isoform 4 [UniParc]. Checksum: 9CD5C12DCF509A50	FASTA	828	93,924
	10 20 30 40 50 60 MDQSVAIQET LAEGEYCVIA VQGVLCEGDS RQSRLLGLVR YRLEHGGQEH ALFLYTHRRM 70 80 90 100 110 120 AITGDDVSLD QIVPVSRDFT LEEVSPDGEL YILGSDVTVQ LDTAELSLVF QLPFGSQTRM 130 140 150 160 170 180 FLHEVARACP GFDSATRDPE FLWLSRYRCA ELELEMPTPR GCNSALVTWP GYATIGGGRY 190 200 210 220 230 240 PSRKKRWGLE EARPQGAGSV LFWGGAMEKT GFRLMERAHG GGFVWGRSAR DGRRDEELEE 250 260 270 280 290 300 AGREMSAAAG SRERNTAGGS NFDGLRPNGK GVPMDQSSRG QDKPESLQPR QNKSKSEITD 310 320 330 340 350 360 MVRSSTITVS DKAHILSMQK FGLRDTIVKS HLLQKEEDYT YIQNFRFFAG TYNVNGQSPK 370 380 390 400 410 420 ECLRLWLSNG IQAPDVYCVG FQELDLSKEA FFFHDTPKEE EWFKAVSEGL HPDAKYAKVK 430 440 450 460 470 480 LIRLVGIMLL LYVKQEHAAY ISEVEAETVG TGIMGRMGNK GGVAIRFQFH NTSICVVNSH 490 500 510 520 530 540 LAAHIEEYER RNQDYKDICS RMQFCQPDPS LPPLTISNHD VILWLGDLNY RIEELDVEKV 550 560 570 580 590 600 KKLIEEKDFQ MLYAYDQLKI QVAAKTVFEG FTEGELTFQP TYKYDTGSDD WDTSEKCRAP 610 620 630 640 650 660 AWCDRILWKG KNITQLSYQS HMALKTSDHK PVSSVFDIGV RVVNDELYRK TLEEIVRSLD 670 680 690 700 710 720 KMENANIPSV SLSKREFCFQ NVKYMQLKVE SFTIHNGQVP CHFEFINKPD EESYCKQWLN 730 740 750 760 770 780 ANPSRGFLLP DSDVEIDLEL FVNKMTATKL NSGEDKIEDI LVLHLDRGKD YFLSVSGNYL 790 800 810 820 PSCFGSPIHT LCYMREPILD LPLETISELL AYLAAYCFET QLVTKSLI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Properties of type II inositol polyphosphate 5-phosphatase." Jefferson A.B., Majerus P.W. J. Biol. Chem. 270:9370-9377(1995) [PubMed: 7721860] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAT LOCATION, ISOPRENYLATION AT CYS-990, MUTAGENESIS OF CYS-990, VARIANT THR-745.
[2]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT THR-745. Tissue: Lymph.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-178. Tissue: Stomach.
[5]	"Cloning and expression of human 75-kDa inositol polyphosphate-5-phosphatase." Ross T.S., Jefferson A.B., Mitchell C.A., Majerus P.W. J. Biol. Chem. 266:20283-20289(1991) [PubMed: 1718960] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 284-954, PROTEIN SEQUENCE OF 321-339, VARIANT THR-745. Tissue: Placenta.
[6]	"Two closely related endocytic proteins that share a common OCRL-binding motif with APPL1." Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P. Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010) [PubMed: 20133602] [Abstract] Cited for: INTERACTION WITH FAM109A.
[7]	"The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling in the endocytic pathway." Noakes C.J., Lee G., Lowe M. Mol. Biol. Cell 22:606-623(2011) [PubMed: 21233288] [Abstract] Cited for: INTERACTION WITH FAM109A AND FAM109B.
[8]	"Crystal structure of INPP5B in complex with phosphatidylinositol 4-phosphate (CASP target)." Structural genomics consortium (SGC) Submitted (JUL-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 339-646 IN COMPLEX WITH PHOSPHATIDYLINOSITOL 4-PHOSPHATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M74161 mRNA. Translation: AAA79207.1. Different initiation.
AL603790, AL929472 Genomic DNA. Translation: CAH69926.1.
AL603790, AL929472 Genomic DNA. Translation: CAH69928.1.
AL603790, AL929472 Genomic DNA. Translation: CAH69929.1.
AL929472, AL603790 Genomic DNA. Translation: CAH70076.1.
AL929472, AL603790 Genomic DNA. Translation: CAH70079.1.
AL929472, AL603790 Genomic DNA. Translation: CAH70080.1.
BX296560 Genomic DNA. No translation available.
BC042529 mRNA. Translation: AAH42529.2.
BC058932 mRNA. Translation: AAH58932.1.
AL833055 mRNA. Translation: CAH56301.1.

IPI

IPI00244111.
IPI00478376.
IPI00553072.
IPI00604769.

RefSeq

NP_005531.2. NM_005540.2.

UniGene

Hs.449942.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3MTC	X-ray	2.40	A	339-643	[»]
3N9V	X-ray	2.65	A/B	342-646	[»]

ProteinModelPortal

P32019.

SMR

P32019. Positions 1-155, 339-643, 656-992.

ModBase

Search...

Protein-protein interaction databases

STRING

P32019.

PTM databases

PhosphoSite

P32019.

Polymorphism databases

DMDM

281185510.

Proteomic databases

PRIDE

P32019.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000373023; ENSP00000362114; ENSG00000204084.
ENST00000373026; ENSP00000362117; ENSG00000204084.

GeneID

3633.

KEGG

hsa:3633.

UCSC

uc001ccf.1. human.
uc001ccg.1. human.
uc009vvk.1. human.

Organism-specific databases

CTD

3633.

GeneCards

GC01M038326.

H-InvDB

HIX0199823.

HGNC

HGNC:6077. INPP5B.

HPA

HPA028803.

MIM

147264. gene.

neXtProt

NX_P32019.

PharmGKB

PA29885.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG04448.

GeneTree

ENSGT00590000082823.

HOVERGEN

HBG000070.

InParanoid

P32019.

OMA

GVAIRFQ.

PhylomeDB

P32019.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000134678-MONOMER.

BRENDA

3.1.3.36. 2681.

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P32019.

Bgee

P32019.

CleanEx

HS_INPP5B.

Genevestigator

P32019.

GermOnline

ENSG00000204084. Homo sapiens.

Family and domain databases

InterPro

IPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]

Gene3D

G3DSA:1.10.555.10. RhoGAP. 1 hit.

KO

K01099.

Pfam

PF03372. Exo_endo_phos. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]

SMART

SM00128. IPPc. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]

SUPFAM

SSF56219. Exo_endo_phos. 1 hit.
SSF48350. Rho_GAP. 1 hit.

PROSITE

PS50238. RHOGAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

14219.

SOURCE

Search...

Entry information

Entry name

I5P2_HUMAN

Accession

Primary (citable) accession number: P32019
Secondary accession number(s): C9J6U5 , Q5VSG9, Q5VSH0, Q5VSH1, Q658Q5, Q6P6D4, Q6PD53, Q86YE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	December 15, 2009
Last modified:	January 25, 2012
This is version 112 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.